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Volumn 265, Issue 2, 1999, Pages 308-318

Bovine leukemia virus Gag particle assembly in insect cells: Formation of chimeric particles by domain-switched leukemia/lentivirus Gag polyprotein

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; CHIMERIC PROTEIN; GENE PRODUCT; NUCLEOCAPSID PROTEIN; PROTEIN PRECURSOR; VIRUS PROTEIN;

EID: 0033590187     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.0007     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins
    • Bennett R. P., Nelle T. D., Wills J. W. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins. J. Virol. 67:1993;6487-6498.
    • (1993) J. Virol. , vol.67 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 2
    • 0030422950 scopus 로고    scopus 로고
    • Use of heterologous expression systems to study retroviral morphogenesis
    • Boulanger P., Jones I. M. Use of heterologous expression systems to study retroviral morphogenesis. Curr. Top. Microbiol. Immunol. 214:1996;237-260.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 237-260
    • Boulanger, P.1    Jones, I.M.2
  • 3
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of HIV-1
    • Bryant M., Ratner L. Myristoylation-dependent replication and assembly of HIV-1. Proc. Natl. Acad. Sci. USA. 87:1990;523-527.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 5
    • 0028916064 scopus 로고
    • Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 MA Gag precursor into retrovirus-like particles
    • Carriere C., Gay B., Chazal N., Morin N., Boulanger P. Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 MA Gag precursor into retrovirus-like particles. J. Virol. 69:1995;2366-2377.
    • (1995) J. Virol. , vol.69 , pp. 2366-2377
    • Carriere, C.1    Gay, B.2    Chazal, N.3    Morin, N.4    Boulanger, P.5
  • 6
    • 0030596149 scopus 로고    scopus 로고
    • Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses
    • Christensen A. M., Massian M. A., Turner B. G., Sundquist W. I., Summers M. F. Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses. J. Mol. Biol. 264:1996;1117-1131.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1117-1131
    • Christensen, A.M.1    Massian, M.A.2    Turner, B.G.3    Sundquist, W.I.4    Summers, M.F.5
  • 7
    • 0030869124 scopus 로고    scopus 로고
    • The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly
    • Conte M. R., Kikova M., Hunter E., Ruml T., Matthews S. The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly. EMBO J. 16:1997;5819-5826.
    • (1997) EMBO J. , vol.16 , pp. 5819-5826
    • Conte, M.R.1    Kikova, M.2    Hunter, E.3    Ruml, T.4    Matthews, S.5
  • 8
    • 0032486598 scopus 로고    scopus 로고
    • Retroviral matrix proteins: A structural perspective
    • Conte M. R., Matthews S. Retroviral matrix proteins: A structural perspective. Virology. 246:1998;191-198.
    • (1998) Virology , vol.246 , pp. 191-198
    • Conte, M.R.1    Matthews, S.2
  • 10
    • 0019858779 scopus 로고
    • Experiments with cloned complete tumor-derived bovine leukemia virus information prove that the virus is totally exogenous to its target animal species
    • Deschamps J., Kettmann R., Burny A. Experiments with cloned complete tumor-derived bovine leukemia virus information prove that the virus is totally exogenous to its target animal species. J. Virol. 40:1981;605-609.
    • (1981) J. Virol. , vol.40 , pp. 605-609
    • Deschamps, J.1    Kettmann, R.2    Burny, A.3
  • 11
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type I
    • Dorfman T., Bukovsky A., Ohagen A., Hoglund S., Gottlinger H. Functional domains of the capsid protein of human immunodeficiency virus type I. J. Virol. 68:1994;8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.5
  • 12
    • 0028363103 scopus 로고
    • Specificity and sequence requirements for interactions between various retroviral Gag proteins
    • Franke E. K., Yuan H. E., Bossolt K. L., Goff S. P., Luban J. Specificity and sequence requirements for interactions between various retroviral Gag proteins. J. Virol. 68:1994;5300-5305.
    • (1994) J. Virol. , vol.68 , pp. 5300-5305
    • Franke, E.K.1    Yuan, H.E.2    Bossolt, K.L.3    Goff, S.P.4    Luban, J.5
  • 13
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • Freed E. O. HIV-1 Gag proteins: Diverse functions in the virus life cycle. Virology. 251:1998;1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 14
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55 Gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen D., Jacobs E., Foresta F., Yhiriart C., Francotte M., Thines D., De Wilde M. Assembly and release of HIV-1 precursor Pr55 Gag virus-like particles from recombinant baculovirus-infected insect cells. Cell. 59:1989;103-112.
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    Foresta, F.3    Yhiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 15
    • 0032529508 scopus 로고    scopus 로고
    • The matrix protein of HIV-1 is not sufficient for assembly and release of virus-like particles
    • Giddings A. M., Ritter G. D., Mulligan M. J. The matrix protein of HIV-1 is not sufficient for assembly and release of virus-like particles. Virology. 248:1998;108-116.
    • (1998) Virology , vol.248 , pp. 108-116
    • Giddings, A.M.1    Ritter, G.D.2    Mulligan, M.J.3
  • 16
    • 0027198787 scopus 로고
    • Assembly of the matrix protein of simian immunodeficiency virus into virus-like particles
    • Gonzalez S. A., Affranchino J. L., Gelderblom H. R., Burny A. Assembly of the matrix protein of simian immunodeficiency virus into virus-like particles. Virology. 194:1993;548-556.
    • (1993) Virology , vol.194 , pp. 548-556
    • Gonzalez, S.A.1    Affranchino, J.L.2    Gelderblom, H.R.3    Burny, A.4
  • 17
    • 0342394457 scopus 로고
    • Role of the capsid precursor processing and myristoylation in morphogenesis and infectivity of HIV type 1
    • Gottlinger H. G., Sodroski J. G., Haseltine W. A. Role of the capsid precursor processing and myristoylation in morphogenesis and infectivity of HIV type 1. Proc. Natl. Acad. Sci. USA. 86:1989;5781-5785.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 18
    • 0027953989 scopus 로고
    • Retrovirus-like particles produced by vaccinia viruses expressing gag-pro-pol region genes of bovine leukaemia virus
    • Hertig C., Pye A. D., Hyatt A. D., Boyle D. B. Retrovirus-like particles produced by vaccinia viruses expressing gag-pro-pol region genes of bovine leukaemia virus. J. Gen. Virol. 75:1994;2213-2221.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2213-2221
    • Hertig, C.1    Pye, A.D.2    Hyatt, A.D.3    Boyle, D.B.4
  • 19
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • Hill C. P., Worthylake D., Bancroft D. P., Christensen A. M., Sundquist W. I. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly. Proc. Natl. Acad. Sci. USA. 93:1996;3099-3104.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 21
    • 0027243846 scopus 로고
    • Morphogenic capabilities of human immunodeficiency virus type-1 gag and gag-pol proteins in insect cells
    • Hughes B. P., Booth T. F., Belyaev A. S., McIlroy D., Jowett J., Roy P. Morphogenic capabilities of human immunodeficiency virus type-1 gag and gag-pol proteins in insect cells. Virology. 193:1993;242-255.
    • (1993) Virology , vol.193 , pp. 242-255
    • Hughes, B.P.1    Booth, T.F.2    Belyaev, A.S.3    McIlroy, D.4    Jowett, J.5    Roy, P.6
  • 22
    • 0002168907 scopus 로고
    • Macromolecular interactions in the assembly of HIV and other retroviruses
    • Hunter E. Macromolecular interactions in the assembly of HIV and other retroviruses. Semin. Virol. 5:1994;71-83.
    • (1994) Semin. Virol. , vol.5 , pp. 71-83
    • Hunter, E.1
  • 25
    • 0027273755 scopus 로고
    • A method for producing recombinant baculovirus expression vectors at high frequency
    • Kitts P. A., Possee R. D. A method for producing recombinant baculovirus expression vectors at high frequency. BioTechniques. 14:1993;810-816.
    • (1993) BioTechniques , vol.14 , pp. 810-816
    • Kitts, P.A.1    Possee, R.D.2
  • 26
    • 0030465377 scopus 로고    scopus 로고
    • Comparison of the NMR and X-ray structures of the HIV-1 matrix protein: Evidence for conformational changes during viral assembly
    • Massiah M. A., Worthylake D., Christensen A. M., Sundquist W. I., Hill C. P., Summers M. F. Comparison of the NMR and X-ray structures of the HIV-1 matrix protein: Evidence for conformational changes during viral assembly. Protein Sci. 5:1996;2391-2398.
    • (1996) Protein Sci. , vol.5 , pp. 2391-2398
    • Massiah, M.A.1    Worthylake, D.2    Christensen, A.M.3    Sundquist, W.I.4    Hill, C.P.5    Summers, M.F.6
  • 27
    • 0023091932 scopus 로고
    • Baculovirus expression vectors: The requirements for high level expression of proteins, including glycoproteins
    • Matsuura Y., Possee R. D., Overton H. A., Bishop D. H. L. Baculovirus expression vectors: The requirements for high level expression of proteins, including glycoproteins. J. Gen. Virol. 68:1987;1233-1250.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1233-1250
    • Matsuura, Y.1    Possee, R.D.2    Overton, H.A.3    Bishop, D.H.L.4
  • 28
    • 0030035221 scopus 로고    scopus 로고
    • The solution structure of the bovine leukaemia virus matrix protein and similarity with lentiviral matrix proteins
    • Matthews S., Mikhailov M., Burny A., Roy P. The solution structure of the bovine leukaemia virus matrix protein and similarity with lentiviral matrix proteins. EMBO J. 15:1996;3267-3274.
    • (1996) EMBO J. , vol.15 , pp. 3267-3274
    • Matthews, S.1    Mikhailov, M.2    Burny, A.3    Roy, P.4
  • 29
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral construct in mammalian cells
    • Mergener K., Facke M., Welker R., Brinkmann V., Gelderblom H. R., Krausslich H. G. Analysis of HIV particle formation using transient expression of subviral construct in mammalian cells. Virology. 186:1992;25-39.
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Facke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Krausslich, H.G.6
  • 30
    • 0025879130 scopus 로고
    • Analyses of the requirements for the synthesis of virus-like particles by feline immunodeficiency virus gag using baculovirus vectors
    • Morikawa S., Booth T. F., Bishop D. H. L. Analyses of the requirements for the synthesis of virus-like particles by feline immunodeficiency virus gag using baculovirus vectors. Virology. 183:1991;288-297.
    • (1991) Virology , vol.183 , pp. 288-297
    • Morikawa, S.1    Booth, T.F.2    Bishop, D.H.L.3
  • 31
    • 0029051459 scopus 로고
    • A molecular determinant of human immunodeficiency virus particle assembly located in the antigen p17
    • Morikawa Y., Kishi T., Zhang W. H., Nermut M. V., Hockley D. J., Jones I. M. A molecular determinant of human immunodeficiency virus particle assembly located in the antigen p17. J. Virol. 69:1995;4519-4523.
    • (1995) J. Virol. , vol.69 , pp. 4519-4523
    • Morikawa, Y.1    Kishi, T.2    Zhang, W.H.3    Nermut, M.V.4    Hockley, D.J.5    Jones, I.M.6
  • 32
    • 0031870255 scopus 로고    scopus 로고
    • Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17
    • Morikawa Y., Zhang W. H., Hockley D. J., Nermut M. V., Jones I. M. Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17. J. Virol. 72:1998;7659-7663.
    • (1998) J. Virol. , vol.72 , pp. 7659-7663
    • Morikawa, Y.1    Zhang, W.H.2    Hockley, D.J.3    Nermut, M.V.4    Jones, I.M.5
  • 33
    • 0030407681 scopus 로고    scopus 로고
    • Comparative morphology and structural classification of retroviruses
    • Nermut M. V., Hockley D. J. Comparative morphology and structural classification of retroviruses. Curr. Top. Microbiol. Immunol. 214:1996;1-24.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 1-24
    • Nermut, M.V.1    Hockley, D.J.2
  • 34
    • 0031731459 scopus 로고    scopus 로고
    • Further evidence for hexagonal organization of HIV Gag protein in prebudding assemblies and immature virus-like particles
    • Nermut M. V., Hockley D. J., Bron P., Thomas D., Zhang W. H., Jones I. M. Further evidence for hexagonal organization of HIV Gag protein in prebudding assemblies and immature virus-like particles. J. Struct. Biol. 123:1998;143-149.
    • (1998) J. Struct. Biol. , vol.123 , pp. 143-149
    • Nermut, M.V.1    Hockley, D.J.2    Bron, P.3    Thomas, D.4    Zhang, W.H.5    Jones, I.M.6
  • 35
    • 0028292220 scopus 로고
    • Fullerene-like organization of HIV Gag protein shell in virus-like particles produced by recombinant baculovirus
    • Nermut M. V., Hockley D. J., Jowett J. B. M., Jones I. M., Garreau M., Thomas D. Fullerene-like organization of HIV Gag protein shell in virus-like particles produced by recombinant baculovirus. Virology. 198:1994;288-296.
    • (1994) Virology , vol.198 , pp. 288-296
    • Nermut, M.V.1    Hockley, D.J.2    Jowett, J.B.M.3    Jones, I.M.4    Garreau, M.5    Thomas, D.6
  • 38
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • Rao Z., Belyaev A. S., Fry E., Roy P., Jones I. M., Stuart D. I. Crystal structure of SIV matrix antigen and implications for virus assembly. Nature. 378:1995;743-747.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jones, I.M.5    Stuart, D.I.6
  • 39
    • 0025107172 scopus 로고
    • Characterization of virus-like particles produced by a recombinant baculovirus containing the gag gene of the bovine immunodeficiency-like virus
    • Rasmussen L., Battles J. K., Ennis W. H., Nagashima K., Gonda M. A. Characterization of virus-like particles produced by a recombinant baculovirus containing the gag gene of the bovine immunodeficiency-like virus. Virology. 178:1990;435-451.
    • (1990) Virology , vol.178 , pp. 435-451
    • Rasmussen, L.1    Battles, J.K.2    Ennis, W.H.3    Nagashima, K.4    Gonda, M.A.5
  • 40
    • 0022794486 scopus 로고
    • Myristoylation site in Pr65Gag is essential for virus particle formation by Moloney murine leukemia virus
    • Rein A., McClure M. R., Rice N. R., Luftig R. B., Schultz A. M. Myristoylation site in Pr65Gag is essential for virus particle formation by Moloney murine leukemia virus. Proc. Natl. Acad. Sci. USA. 83:1986;7246-7250.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7246-7250
    • Rein, A.1    McClure, M.R.2    Rice, N.R.3    Luftig, R.B.4    Schultz, A.M.5
  • 41
    • 0023109641 scopus 로고
    • Myristoylation is required for intracellular transport but not for assembly of D-type retrovirus capsids
    • Rhee S. S., Hunter E. Myristoylation is required for intracellular transport but not for assembly of D-type retrovirus capsids. J. Virol. 61:1987;1045-1053.
    • (1987) J. Virol. , vol.61 , pp. 1045-1053
    • Rhee, S.S.1    Hunter, E.2
  • 42
    • 0011310662 scopus 로고
    • Complete nucleotide sequence of the genome of bovine leukemia virus: Its evolutionary relationship to other retroviruses
    • Sagata N., Yasunaga T., Tsuzuku Kawamura J., Ohishi K., Ogawa Y., Ikawa Y. Complete nucleotide sequence of the genome of bovine leukemia virus: Its evolutionary relationship to other retroviruses. Proc. Natl. Acad. Sci. USA. 82:1985;677-681.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 677-681
    • Sagata, N.1    Yasunaga, T.2    Tsuzuku Kawamura, J.3    Ohishi, K.4    Ogawa, Y.5    Ikawa, Y.6
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitro-cellulose sheets: Procedure and some applications
    • Towbin H., Staehalin T., Godon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitro-cellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehalin, T.2    Godon, J.3
  • 47
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Wills J., Craven R. Form, function, and use of retroviral gag proteins. AIDS. 5:1991;639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.1    Craven, R.2
  • 48
    • 0026715925 scopus 로고
    • The matrix protein of HIV-1 is required for incorporation of viral envelope protein into mature virions
    • Yu X., Yuan X., Matsuda Z., Lee T. H., Essex M. The matrix protein of HIV-1 is required for incorporation of viral envelope protein into mature virions. J. Virol. 66:1992;4966-4971.
    • (1992) J. Virol. , vol.66 , pp. 4966-4971
    • Yu, X.1    Yuan, X.2    Matsuda, Z.3    Lee, T.H.4    Essex, M.5
  • 49
    • 0030007245 scopus 로고    scopus 로고
    • Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly
    • Zhang W. H., Hockley D. J., Nermut M. V., Morikawa Y., Jones I. M. Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly. J. Gen. Virol. 77:1996;743-751.
    • (1996) J. Gen. Virol. , vol.77 , pp. 743-751
    • Zhang, W.H.1    Hockley, D.J.2    Nermut, M.V.3    Morikawa, Y.4    Jones, I.M.5


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